1887

Abstract

The degradation of the foreign protein [C]methyl apohaemoglobin ([C-me]globin) was stimulated by ATP in cell-free extracts from exponential phase and shaken and standing stationary phase cells. A marked stimulation by ATP of the degradation of [C-me]globin was observed with exponential phase cell extracts which were preincubated for 30 min at 30 °C. Maximum stimulation was obtained with 3 m-ATP and optimum degradation was at pH 8·0–8·5. Preincubation of extracts from both types of stationary phase cells did not affect the degree of ATP stimulation. The amount of ATP stimulation of [C-me]globin degradation by exponential phase extracts decreased markedly when the cells were starved in a growth limiting minimal medium before preparation of the cell extracts. In the exponential and both types of stationary phase extracts most of the activity was located in the cytoplasmic fractions. Although the periplasmic preparations contained a minor portion of the total activity, this activity showed a greater percentage stimulation by ATP. In the absence of ATP the specific proteolytic activities of the extracts from exponential and both types of stationary phase cells were similar. The proteolytic activities in all the cell extracts were inhibited to the same extent by phenylmethylsulphonyl fluoride, but the exponential and both types of stationary phase cell extracts were inhibited to different extents by EDTA and -hydroxymercuribenzoate. The results suggest that the proteolytic systems responsible for the degradation of abnormal proteins are different in exponential and stationary phase cells.

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/content/journal/micro/10.1099/00221287-130-11-2775
1984-11-01
2024-04-19
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References

  1. Etlinoer J., Goldberg A.L. 1977; A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes. Proceedings of the National Academy of Sciences of the United States of America 74:54–58
    [Google Scholar]
  2. Goldberg A.L., Dice J.F. 1974; Intracellular protein degradation in mammalian and bacterial cells. Annual Review of Biochemistry 43:835–869
    [Google Scholar]
  3. Hall B., Gallant J. 1972; Defective translation in RC#x2212; cells. Nature New Biology 237:131–135
    [Google Scholar]
  4. Kaback H.R. 1971; Bacterial membranes. In Enzyme Purification and Related Techniques XXII pp. 99–120 Jackboy W.B. Edited by New york: Academic press;
    [Google Scholar]
  5. Kowrr J.D., Goldberg A.L. 1977; Intermediate steps in the degradation of a specific abnormal protein in Escherichia coli. Journal of Biological Chemistry 252:8350–8357
    [Google Scholar]
  6. Liu C.-J., Chopra A.K., Strnadova M., Chaloupka J. 1984; Degradation of abnormal proteins in growing yeast. FEMS Microbiology Letters 21:313–317
    [Google Scholar]
  7. Murakami K., Voellmy R., Goldberg A.L. 1979; Protein degradation is stimulated by ATP in extracts of Escherichia coli. Journal of Biological Chemistry 254:8194–8200
    [Google Scholar]
  8. Rice R.H., Means G.E. 1971; Radioactive labelling of proteins in vitro. Journal of Biological Chemistry 246:831–832
    [Google Scholar]
  9. Robb S.M., Woods D.R., Robb F.T., Struthers J.K. 1977; Rifampicin-resistant mutant supporting bacteriophage growth on stationary phase Achromobacter cells. Journal of General Virology 35:117–123
    [Google Scholar]
  10. Robb S.M., Woods D.R., Robb F.T. 1978; Phage growth characteristics on stationary phase Achromobacter cells. Journal of General Virology 41:265–272
    [Google Scholar]
  11. Robb S.M., Robb F.T., Woods D.R. 1980; Physiological and morphological characteristics of stationary phase Vibrio cells able to support phage growth. Journal of General Microbiology 119:405–412
    [Google Scholar]
  12. St John A.C., Goldberg A.L. 1978; Effects of reduced energy production on protein degradation, guanosine tetraphosphate, and RNA synthesis in Escherichia coli. Journal of Biological Chemistry 253:2705–2711
    [Google Scholar]
  13. Thomson J.A., Woods D.R. 1974; Bacteriophages and cryptic lysogeny in Achromobacter. Journal of General Virology 22:153–157
    [Google Scholar]
  14. Travers A.A. 1976; RNA polymerase specificity and the control of growth. London: Nature; 263641–646
    [Google Scholar]
  15. Wickner W., Brutlag D., Schekman R., Korn-Berg A. 1972; RNA synthesis initiates in vitro conversion of Ml3 DNA to its replicative form. Proceedings of the National Academy of Sciences of the United States of America 69:965–969
    [Google Scholar]
  16. Woods D.R. 1976; Bacteriophage growth on stationary phase Achromobacter cells. Journal of General Virology 32:45–50
    [Google Scholar]
  17. Yonetani T. 1967; Crystalline apo- and reconstituted holoenzymes. Journal of Biological Chemistry 242:5008–5013
    [Google Scholar]
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